RHO_MYCTU
ID RHO_MYCTU Reviewed; 602 AA.
AC P9WHF3; L0T8Z1; P66028; Q10607;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 41.
DE RecName: Full=Transcription termination factor Rho {ECO:0000255|HAMAP-Rule:MF_01884};
DE EC=3.6.4.- {ECO:0000255|HAMAP-Rule:MF_01884};
DE AltName: Full=ATP-dependent helicase Rho {ECO:0000255|HAMAP-Rule:MF_01884};
GN Name=rho {ECO:0000255|HAMAP-Rule:MF_01884}; OrderedLocusNames=Rv1297;
GN ORFNames=MTCY373.17;
OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83332;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=9634230; DOI=10.1038/31159;
RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA Barrell B.G.;
RT "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT genome sequence.";
RL Nature 393:537-544(1998).
RN [2]
RP IDENTIFICATION AS A DRUG TARGET [LARGE SCALE ANALYSIS].
RX PubMed=19099550; DOI=10.1186/1752-0509-2-109;
RA Raman K., Yeturu K., Chandra N.;
RT "targetTB: a target identification pipeline for Mycobacterium tuberculosis
RT through an interactome, reactome and genome-scale structural analysis.";
RL BMC Syst. Biol. 2:109-109(2008).
RN [3]
RP FUNCTION, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, AND
RP DOMAIN.
RX PubMed=20026069; DOI=10.1016/j.jmb.2009.12.022;
RA Kalarickal N.C., Ranjan A., Kalyani B.S., Wal M., Sen R.;
RT "A bacterial transcription terminator with inefficient molecular motor
RT action but with a robust transcription termination function.";
RL J. Mol. Biol. 395:966-982(2010).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT mass spectrometry.";
RL Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
CC -!- FUNCTION: Facilitates transcription termination by a mechanism that
CC involves Rho binding to the nascent RNA, activation of Rho's RNA-
CC dependent ATPase activity, and release of the mRNA from the DNA
CC template. Shows poor RNA-dependent ATP hydrolysis and inefficient DNA-
CC RNA unwinding activities, but exhibits robust and fast transcription
CC termination, which suggests that the transcription termination function
CC of M.tuberculosis Rho is not correlated with its helicase/translocase
CC activities and that these functions may not be important for its RNA
CC release process. {ECO:0000255|HAMAP-Rule:MF_01884,
CC ECO:0000269|PubMed:20026069}.
CC -!- ACTIVITY REGULATION: The antibiotic bicyclomycin inhibits ATPase
CC activity but does not affect termination function.
CC {ECO:0000269|PubMed:20026069}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=70 uM for ATP {ECO:0000269|PubMed:20026069};
CC -!- SUBUNIT: Homohexamer. The homohexamer assembles into an open ring
CC structure. Does not bind NusG. {ECO:0000255|HAMAP-Rule:MF_01884,
CC ECO:0000269|PubMed:20026069}.
CC -!- DOMAIN: Contains an extra N-terminal domain, a S1-like RNA-binding
CC domain and a conserved P-loop NTPase domain.
CC {ECO:0000269|PubMed:20026069}.
CC -!- MISCELLANEOUS: Was identified as a high-confidence drug target.
CC -!- SIMILARITY: Belongs to the Rho family. {ECO:0000255|HAMAP-
CC Rule:MF_01884}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AL123456; CCP44054.1; -; Genomic_DNA.
DR PIR; E70773; E70773.
DR RefSeq; NP_215813.1; NC_000962.3.
DR RefSeq; WP_003898814.1; NZ_NVQJ01000030.1.
DR AlphaFoldDB; P9WHF3; -.
DR SMR; P9WHF3; -.
DR STRING; 83332.Rv1297; -.
DR PaxDb; P9WHF3; -.
DR DNASU; 886952; -.
DR GeneID; 45425271; -.
DR GeneID; 886952; -.
DR KEGG; mtu:Rv1297; -.
DR TubercuList; Rv1297; -.
DR eggNOG; COG1158; Bacteria.
DR OMA; TKDANDH; -.
DR PhylomeDB; P9WHF3; -.
DR SABIO-RK; P9WHF3; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0009274; C:peptidoglycan-based cell wall; HDA:MTBBASE.
DR GO; GO:0005886; C:plasma membrane; HDA:MTBBASE.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0008186; F:ATP-dependent activity, acting on RNA; IEA:InterPro.
DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006363; P:termination of RNA polymerase I transcription; IDA:MTBBASE.
DR CDD; cd01128; rho_factor; 1.
DR Gene3D; 2.40.50.140; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR HAMAP; MF_01884; Rho; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR000194; ATPase_F1/V1/A1_a/bsu_nucl-bd.
DR InterPro; IPR011129; CSD.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR041703; Rho_factor_ATP-bd.
DR InterPro; IPR011112; Rho_N.
DR InterPro; IPR036269; Rho_N_sf.
DR InterPro; IPR011113; Rho_RNA-bd.
DR InterPro; IPR004665; Term_rho.
DR PANTHER; PTHR46425; PTHR46425; 1.
DR Pfam; PF00006; ATP-synt_ab; 1.
DR Pfam; PF07498; Rho_N; 1.
DR Pfam; PF07497; Rho_RNA_bind; 1.
DR SMART; SM00382; AAA; 1.
DR SMART; SM00357; CSP; 1.
DR SMART; SM00959; Rho_N; 1.
DR SUPFAM; SSF50249; SSF50249; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF68912; SSF68912; 1.
DR TIGRFAMs; TIGR00767; rho; 1.
DR PROSITE; PS51856; RHO_RNA_BD; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Helicase; Hydrolase; Nucleotide-binding; Reference proteome;
KW RNA-binding; Transcription; Transcription regulation;
KW Transcription termination.
FT CHAIN 1..602
FT /note="Transcription termination factor Rho"
FT /id="PRO_0000188970"
FT DOMAIN 223..301
FT /note="Rho RNA-BD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01203"
FT REGION 1..35
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 76..216
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 100..122
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 151..167
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 344..349
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01884"
FT BINDING 356..361
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01884"
FT BINDING 387
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01884"
SQ SEQUENCE 602 AA; 65133 MW; 4E77B200810AE57F CRC64;
MTDTDLITAG ESTDGKPSDA AATDPPDLNA DEPAGSLATM VLPELRALAN RAGVKGTSGM
RKNELIAAIE EIRRQANGAP AVDRSAQEHD KGDRPPSSEA PATQGEQTPT EQIDSQSQQV
RPERRSATRE AGPSGSGERA GTAADDTDNR QGGQQDAKTE ERGTDAGGDQ GGDQQASGGQ
QARGDEDGEA RQGRRGRRFR DRRRRGERSG DGAEAELRED DVVQPVAGIL DVLDNYAFVR
TSGYLPGPHD VYVSMNMVRK NGMRRGDAVT GAVRVPKEGE QPNQRQKFNP LVRLDSINGG
SVEDAKKRPE FGKLTPLYPN QRLRLETSTE RLTTRVIDLI MPIGKGQRAL IVSPPKAGKT
TILQDIANAI TRNNPECHLM VVLVDERPEE VTDMQRSVKG EVIASTFDRP PSDHTSVAEL
AIERAKRLVE QGKDVVVLLD SITRLGRAYN NASPASGRIL SGGVDSTALY PPKRFLGAAR
NIEEGGSLTI IATAMVETGS TGDTVIFEEF KGTGNAELKL DRKIAERRVF PAVDVNPSGT
RKDELLLSPD EFAIVHKLRR VLSGLDSHQA IDLLMSQLRK TKNNYEFLVQ VSKTTPGSMD
SD
